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Database: UniProt
Entry: P26038
LinkDB: P26038
Original site: P26038 
ID   MOES_HUMAN              Reviewed;         577 AA.
AC   P26038;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   23-FEB-2022, entry version 234.
DE   RecName: Full=Moesin {ECO:0000303|PubMed:1924289};
DE   AltName: Full=Membrane-organizing extension spike protein;
GN   Name=MSN {ECO:0000312|HGNC:HGNC:7373};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-16; 54-60 AND
RP   414-435.
RC   TISSUE=Placenta;
RX   PubMed=1924289; DOI=10.1073/pnas.88.19.8297;
RA   Lankes W.T., Furthmayr H.;
RT   "Moesin: a member of the protein 4.1-talin-ezrin family of proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:8297-8301(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA   Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA   Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA   Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA   Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA   Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA   Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA   Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA   Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA   Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA   Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA   Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA   Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA   Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA   Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA   Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA   Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA   Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA   Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA   Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA   Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA   Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA   Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA   Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA   Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA   Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA   Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA   Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA   Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA   Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA   Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA   Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA   d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA   Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA   Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA   Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA   Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA   Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA   Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA   Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pancreas;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-8.
RC   TISSUE=Platelet;
RX   PubMed=12665801; DOI=10.1038/nbt810;
RA   Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA   Vandekerckhove J.;
RT   "Exploring proteomes and analyzing protein processing by mass spectrometric
RT   identification of sorted N-terminal peptides.";
RL   Nat. Biotechnol. 21:566-569(2003).
RN   [5]
RP   INTERACTION WITH CD46, AND SUBCELLULAR LOCATION.
RX   PubMed=7884872; DOI=10.1128/jvi.69.4.2248-2256.1995;
RA   Schneider-Schaulies J., Dunster L.M., Schwartz-Albiez R., Krohne G.,
RA   ter Meulen V.;
RT   "Physical association of moesin and CD46 as a receptor complex for measles
RT   virus.";
RL   J. Virol. 69:2248-2256(1995).
RN   [6]
RP   INTERACTION WITH SLC9A3R1.
RX   PubMed=9314537; DOI=10.1083/jcb.139.1.169;
RA   Reczek D., Berryman M., Bretscher A.;
RT   "Identification of EBP50: a PDZ-containing phosphoprotein that associates
RT   with members of the ezrin-radixin-moesin family.";
RL   J. Cell Biol. 139:169-179(1997).
RN   [7]
RP   INTERACTION WITH HIV-1 ENVELOPE PROTEIN GP120.
RX   PubMed=9213396; DOI=10.1016/s0168-1702(97)00039-7;
RA   Hecker C., Weise C., Schneider-Schaulies J., Holmes H.C., ter Meulen V.;
RT   "Specific binding of HIV-1 envelope protein gp120 to the structural
RT   membrane proteins ezrin and moesin.";
RL   Virus Res. 49:215-223(1997).
RN   [8]
RP   FUNCTION, INTERACTION WITH ICAM3 AND CD44, AND SUBCELLULAR LOCATION.
RX   PubMed=9298994; DOI=10.1083/jcb.138.6.1409;
RA   Serrador J.M., Alonso-Lebrero J.L., del Pozo M.A., Furthmayr H.,
RA   Schwartz-Albiez R., Calvo J., Lozano F., Sanchez-Madrid F.;
RT   "Moesin interacts with the cytoplasmic region of intercellular adhesion
RT   molecule-3 and is redistributed to the uropod of T lymphocytes during cell
RT   polarization.";
RL   J. Cell Biol. 138:1409-1423(1997).
RN   [9]
RP   FUNCTION, AND INTERACTION WITH SPN/CD43 CYTOPLASMIC TAIL.
RX   PubMed=9616160;
RA   Serrador J.M., Nieto M., Alonso-Lebrero J.L., del Pozo M.A., Calvo J.,
RA   Furthmayr H., Schwartz-Albiez R., Lozano F., Gonzalez-Amaro R.,
RA   Sanchez-Mateos P., Sanchez-Madrid F.;
RT   "CD43 interacts with moesin and ezrin and regulates its redistribution to
RT   the uropods of T lymphocytes at the cell-cell contacts.";
RL   Blood 91:4632-4644(1998).
RN   [10]
RP   FUNCTION, MUTAGENESIS OF THR-558, AND INTERACTION WITH F-ACTIN.
RX   PubMed=10212266; DOI=10.1074/jbc.274.18.12803;
RA   Huang L., Wong T.Y., Lin R.C., Furthmayr H.;
RT   "Replacement of threonine 558, a critical site of phosphorylation of moesin
RT   in vivo, with aspartate activates F-actin binding of moesin. Regulation by
RT   conformational change.";
RL   J. Biol. Chem. 274:12803-12810(1999).
RN   [11]
RP   FUNCTION, INTERACTION WITH SPN/CD43 CYTOPLASMIC TAIL, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=11728332; DOI=10.1016/s1074-7613(01)00231-x;
RA   Delon J., Kaibuchi K., Germain R.N.;
RT   "Exclusion of CD43 from the immunological synapse is mediated by
RT   phosphorylation-regulated relocation of the cytoskeletal adaptor moesin.";
RL   Immunity 15:691-701(2001).
RN   [12]
RP   INTERACTION WITH SELPLG AND SYK, AND FUNCTION.
RX   PubMed=12387735; DOI=10.1016/s1074-7613(02)00420-x;
RA   Urzainqui A., Serrador J.M., Viedma F., Yanez-Mo M., Rodriguez A.,
RA   Corbi A.L., Alonso-Lebrero J.L., Luque A., Deckert M., Vazquez J.,
RA   Sanchez-Madrid F.;
RT   "ITAM-based interaction of ERM proteins with Syk mediates signaling by the
RT   leukocyte adhesion receptor PSGL-1.";
RL   Immunity 17:401-412(2002).
RN   [13]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=15039356; DOI=10.1128/iai.72.4.2312-2320.2004;
RA   Iontcheva I., Amar S., Zawawi K.H., Kantarci A., Van Dyke T.E.;
RT   "Role for moesin in lipopolysaccharide-stimulated signal transduction.";
RL   Infect. Immun. 72:2312-2320(2004).
RN   [14]
RP   INTERACTION WITH PDPN.
RX   PubMed=17046996; DOI=10.1242/jcs.03218;
RA   Martin-Villar E., Megias D., Castel S., Yurrita M.M., Vilaro S.,
RA   Quintanilla M.;
RT   "Podoplanin binds ERM proteins to activate RhoA and promote epithelial-
RT   mesenchymal transition.";
RL   J. Cell Sci. 119:4541-4553(2006).
RN   [15]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH PPP1R16B.
RX   PubMed=18586956; DOI=10.1152/ajplung.00325.2007;
RA   Csortos C., Czikora I., Bogatcheva N.V., Adyshev D.M., Poirier C., Olah G.,
RA   Verin A.D.;
RT   "TIMAP is a positive regulator of pulmonary endothelial barrier function.";
RL   Am. J. Physiol. 295:L440-L450(2008).
RN   [16]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [17]
RP   PHOSPHORYLATION AT THR-558, AND MUTAGENESIS OF TYR-556 AND THR-558.
RX   PubMed=19255442; DOI=10.1073/pnas.0805963106;
RA   Belkina N.V., Liu Y., Hao J.J., Karasuyama H., Shaw S.;
RT   "LOK is a major ERM kinase in resting lymphocytes and regulates
RT   cytoskeletal rearrangement through ERM phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:4707-4712(2009).
RN   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-116, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [19]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-79 AND LYS-139, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [20]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [21]
RP   FUNCTION, AND INTERACTION WITH PDZD8.
RX   PubMed=21549406; DOI=10.1016/j.virol.2011.04.006;
RA   Henning M.S., Stiedl P., Barry D.S., McMahon R., Morham S.G., Walsh D.,
RA   Naghavi M.H.;
RT   "PDZD8 is a novel moesin-interacting cytoskeletal regulatory protein that
RT   suppresses infection by herpes simplex virus type 1.";
RL   Virology 415:114-121(2011).
RN   [22]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [23]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74; SER-407 AND SER-527, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [24]
RP   S-NITROSYLATION AT CYS-117, MUTAGENESIS OF ILE-115 AND GLU-120, AND DOMAIN.
RX   PubMed=25417112; DOI=10.1016/j.cell.2014.09.032;
RA   Jia J., Arif A., Terenzi F., Willard B., Plow E.F., Hazen S.L., Fox P.L.;
RT   "Target-selective protein S-nitrosylation by sequence motif recognition.";
RL   Cell 159:623-634(2014).
RN   [25]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [26]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [27]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 4-577.
RX   PubMed=10847681; DOI=10.1016/s0092-8674(00)80836-3;
RA   Pearson M.A., Reczek D., Bretscher A., Karplus P.A.;
RT   "Structure of the ERM protein moesin reveals the FERM domain fold masked by
RT   an extended actin binding tail domain.";
RL   Cell 101:259-270(2000).
RN   [28]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-346.
RX   PubMed=11401550; DOI=10.1021/bi010419h;
RA   Edwards S.D., Keep N.H.;
RT   "The 2.7 A crystal structure of the activated FERM domain of moesin: an
RT   analysis of structural changes on activation.";
RL   Biochemistry 40:7061-7068(2001).
RN   [29]
RP   X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 1-297 IN COMPLEX WITH SLC9A3R1.
RX   PubMed=15020681; DOI=10.1242/jcs.01038;
RA   Finnerty C.M., Chambers D., Ingraffea J., Faber H.R., Karplus P.A.,
RA   Bretscher A.;
RT   "The EBP50-moesin interaction involves a binding site regulated by direct
RT   masking on the FERM domain.";
RL   J. Cell Sci. 117:1547-1552(2004).
RN   [30]
RP   VARIANT IMD50 TRP-171, CHARACTERIZATION OF VARIANT IMD50 TRP-171, AND
RP   FUNCTION.
RX   PubMed=27405666; DOI=10.1016/j.jaci.2016.04.032;
RA   Lagresle-Peyrou C., Luce S., Ouchani F., Soheili T.S., Sadek H.,
RA   Chouteau M., Durand A., Pic I., Majewski J., Brouzes C., Lambert N.,
RA   Bohineust A., Verhoeyen E., Cosset F.L., Magerus-Chatinet A.,
RA   Rieux-Laucat F., Gandemer V., Monnier D., Heijmans C., van Gijn M.,
RA   Dalm V.A., Mahlaoui N., Stephan J.L., Picard C., Durandy A., Kracker S.,
RA   Hivroz C., Jabado N., de Saint Basile G., Fischer A., Cavazzana M.,
RA   Andre-Schmutz I.;
RT   "X-linked primary immunodeficiency associated with hemizygous mutations in
RT   the moesin (MSN) gene.";
RL   J. Allergy Clin. Immunol. 138:1681-1689(2016).
CC   -!- FUNCTION: Ezrin-radixin-moesin (ERM) family protein that connects the
CC       actin cytoskeleton to the plasma membrane and thereby regulates the
CC       structure and function of specific domains of the cell cortex. Tethers
CC       actin filaments by oscillating between a resting and an activated state
CC       providing transient interactions between moesin and the actin
CC       cytoskeleton (PubMed:10212266). Once phosphorylated on its C-terminal
CC       threonine, moesin is activated leading to interaction with F-actin and
CC       cytoskeletal rearrangement (PubMed:10212266). These rearrangements
CC       regulate many cellular processes, including cell shape determination,
CC       membrane transport, and signal transduction (PubMed:12387735,
CC       PubMed:15039356). The role of moesin is particularly important in
CC       immunity acting on both T and B-cells homeostasis and self-tolerance,
CC       regulating lymphocyte egress from lymphoid organs (PubMed:9298994,
CC       PubMed:9616160). Modulates phagolysosomal biogenesis in macrophages (By
CC       similarity). Participates also in immunologic synapse formation
CC       (PubMed:27405666). {ECO:0000250|UniProtKB:P26041,
CC       ECO:0000269|PubMed:10212266, ECO:0000269|PubMed:12387735,
CC       ECO:0000269|PubMed:15039356, ECO:0000269|PubMed:27405666,
CC       ECO:0000269|PubMed:9298994, ECO:0000269|PubMed:9616160}.
CC   -!- ACTIVITY REGULATION: A head-to-tail association, of the N-terminal and
CC       C-terminal halves results in a closed conformation (inactive form)
CC       which is incapable of actin or membrane-binding.
CC       {ECO:0000269|PubMed:10212266}.
CC   -!- SUBUNIT: In resting T-cells, part of a PAG1-SLC9A3R1-MSN complex which
CC       is disrupted upon TCR activation. Interacts with SLC9A3R1
CC       (PubMed:9314537, PubMed:15020681). Interacts with PPP1R16B
CC       (PubMed:18586956). Interacts with PDZD8. Interacts with SELPLG and SYK;
CC       these interaction mediate the activation of SYK by SELPLG
CC       (PubMed:12387735). Interacts with PDPN (via cytoplasmic domain); this
CC       interaction activates RHOA and promotes epithelial-mesenchymal
CC       transition (PubMed:17046996). Interacts with SPN/CD43 cytoplasmic tail
CC       (PubMed:9616160, PubMed:11728332). Interacts with CD44
CC       (PubMed:9298994). Interacts with ICAM2 (By similarity). Interacts with
CC       ICAM3 (via C-terminus) (PubMed:9298994). Interacts with PDZD8
CC       (PubMed:21549406). Interacts with F-actin (PubMed:10212266). Interacts
CC       with CD46 (PubMed:7884872). Interacts with PTPN6 (By similarity).
CC       {ECO:0000250|UniProtKB:P26041, ECO:0000269|PubMed:10212266,
CC       ECO:0000269|PubMed:11728332, ECO:0000269|PubMed:12387735,
CC       ECO:0000269|PubMed:15020681, ECO:0000269|PubMed:17046996,
CC       ECO:0000269|PubMed:18586956, ECO:0000269|PubMed:21549406,
CC       ECO:0000269|PubMed:7884872, ECO:0000269|PubMed:9298994,
CC       ECO:0000269|PubMed:9314537, ECO:0000269|PubMed:9616160}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 envelope protein
CC       gp120. {ECO:0000269|PubMed:9213396}.
CC   -!- INTERACTION:
CC       P26038; P16070: CD44; NbExp=6; IntAct=EBI-528768, EBI-490245;
CC       P26038; P25791-3: LMO2; NbExp=3; IntAct=EBI-528768, EBI-11959475;
CC       P26038; Q5S007: LRRK2; NbExp=19; IntAct=EBI-528768, EBI-5323863;
CC       P26038; O14745: SLC9A3R1; NbExp=4; IntAct=EBI-528768, EBI-349787;
CC       P26038; P54274: TERF1; NbExp=2; IntAct=EBI-528768, EBI-710997;
CC       P26038; Q5S006: Lrrk2; Xeno; NbExp=2; IntAct=EBI-528768, EBI-2693710;
CC       P26038; P97820: Map4k4; Xeno; NbExp=2; IntAct=EBI-528768, EBI-644181;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11728332,
CC       ECO:0000269|PubMed:15039356, ECO:0000269|PubMed:18586956,
CC       ECO:0000269|PubMed:7884872, ECO:0000269|PubMed:9298994}; Peripheral
CC       membrane protein {ECO:0000250|UniProtKB:P26041}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P26041}. Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:P26041}. Apical cell membrane
CC       {ECO:0000250|UniProtKB:P26041}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P26041}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P26041}. Cell projection, microvillus membrane
CC       {ECO:0000250|UniProtKB:P26041}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P26041}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P26041}. Cell projection, microvillus
CC       {ECO:0000250|UniProtKB:P26041}. Note=Phosphorylated form is enriched in
CC       microvilli-like structures at apical membrane. Increased cell membrane
CC       localization of both phosphorylated and non-phosphorylated forms seen
CC       after thrombin treatment (By similarity). Localizes at the uropods of T
CC       lymphoblasts. {ECO:0000250|UniProtKB:P26041,
CC       ECO:0000269|PubMed:18586956, ECO:0000269|PubMed:9298994}.
CC   -!- TISSUE SPECIFICITY: In all tissues and cultured cells studied.
CC   -!- DOMAIN: The [IL]-x-C-x-x-[DE] motif is a proposed target motif for
CC       cysteine S-nitrosylation mediated by the iNOS-S100A8/A9
CC       transnitrosylase complex. {ECO:0000305|PubMed:25417112}.
CC   -!- PTM: Phosphorylation on Thr-558 is crucial for the formation of
CC       microvilli-like structures. Phosphorylation by ROCK2 suppresses the
CC       head-to-tail association of the N-terminal and C-terminal halves
CC       resulting in an opened conformation which is capable of actin and
CC       membrane-binding (By similarity). Phosphorylation on Thr-558 by STK10
CC       negatively regulates lymphocyte migration and polarization.
CC       {ECO:0000250, ECO:0000269|PubMed:19255442}.
CC   -!- PTM: S-nitrosylation of Cys-117 is induced by interferon-gamma and
CC       oxidatively-modified low-densitity lipoprotein (LDL(ox)) implicating
CC       the iNOS-S100A8/9 transnitrosylase complex.
CC       {ECO:0000269|PubMed:25417112}.
CC   -!- DISEASE: Immunodeficiency 50 (IMD50) [MIM:300988]: A primary
CC       immunodeficiency disorder characterized by onset of recurrent bacterial
CC       or varicella zoster virus infections in early childhood, profound
CC       lymphopenia, hypogammaglobulinemia, fluctuating monocytopenia and
CC       neutropenia, and a poor immune response to vaccine antigens.
CC       {ECO:0000269|PubMed:27405666}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/MSNID363.html";
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DR   EMBL; M69066; AAA36322.1; -; mRNA.
DR   EMBL; Z98946; CAB46379.1; -; Genomic_DNA.
DR   EMBL; BC017293; AAH17293.1; -; mRNA.
DR   CCDS; CCDS14382.1; -.
DR   PIR; A41289; A41289.
DR   RefSeq; NP_002435.1; NM_002444.2.
DR   PDB; 1E5W; X-ray; 2.70 A; A=2-346.
DR   PDB; 1EF1; X-ray; 1.90 A; A/B=4-297, C/D=488-577.
DR   PDB; 1SGH; X-ray; 3.50 A; A=1-297.
DR   PDB; 6TXQ; X-ray; 1.73 A; AAA=1-346.
DR   PDB; 6TXS; X-ray; 2.20 A; AAA=1-346.
DR   PDBsum; 1E5W; -.
DR   PDBsum; 1EF1; -.
DR   PDBsum; 1SGH; -.
DR   PDBsum; 6TXQ; -.
DR   PDBsum; 6TXS; -.
DR   SMR; P26038; -.
DR   BioGRID; 110584; 173.
DR   DIP; DIP-33841N; -.
DR   IntAct; P26038; 43.
DR   MINT; P26038; -.
DR   STRING; 9606.ENSP00000353408; -.
DR   ChEMBL; CHEMBL4295733; -.
DR   GlyGen; P26038; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P26038; -.
DR   MetOSite; P26038; -.
DR   PhosphoSitePlus; P26038; -.
DR   SwissPalm; P26038; -.
DR   BioMuta; MSN; -.
DR   DMDM; 127234; -.
DR   OGP; P26038; -.
DR   CPTAC; CPTAC-94; -.
DR   EPD; P26038; -.
DR   jPOST; P26038; -.
DR   MassIVE; P26038; -.
DR   PaxDb; P26038; -.
DR   PeptideAtlas; P26038; -.
DR   PRIDE; P26038; -.
DR   ProteomicsDB; 54311; -.
DR   TopDownProteomics; P26038; -.
DR   Antibodypedia; 2774; 1016 antibodies from 43 providers.
DR   CPTC; P26038; 3 antibodies.
DR   DNASU; 4478; -.
DR   Ensembl; ENST00000360270; ENSP00000353408; ENSG00000147065.
DR   GeneID; 4478; -.
DR   KEGG; hsa:4478; -.
DR   MANE-Select; ENST00000360270.7; ENSP00000353408.5; NM_002444.3; NP_002435.1.
DR   CTD; 4478; -.
DR   DisGeNET; 4478; -.
DR   GeneCards; MSN; -.
DR   HGNC; HGNC:7373; MSN.
DR   HPA; ENSG00000147065; Low tissue specificity.
DR   MalaCards; MSN; -.
DR   MIM; 300988; phenotype.
DR   MIM; 309845; gene.
DR   neXtProt; NX_P26038; -.
DR   OpenTargets; ENSG00000147065; -.
DR   Orphanet; 504530; Combined immunodeficiency due to Moesin deficiency.
DR   PharmGKB; PA31178; -.
DR   VEuPathDB; HostDB:ENSG00000147065; -.
DR   eggNOG; KOG3529; Eukaryota.
DR   GeneTree; ENSGT00960000186596; -.
DR   HOGENOM; CLU_003623_6_2_1; -.
DR   InParanoid; P26038; -.
DR   OMA; HVTEPMH; -.
DR   OrthoDB; 627741at2759; -.
DR   PhylomeDB; P26038; -.
DR   TreeFam; TF313935; -.
DR   PathwayCommons; P26038; -.
DR   Reactome; R-HSA-437239; Recycling pathway of L1.
DR   Reactome; R-HSA-8950505; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation.
DR   Reactome; R-HSA-9662360; Sensory processing of sound by inner hair cells of the cochlea.
DR   Reactome; R-HSA-9662361; Sensory processing of sound by outer hair cells of the cochlea.
DR   Reactome; R-HSA-9725370; Signaling by ALK fusions and activated point mutants.
DR   SignaLink; P26038; -.
DR   SIGNOR; P26038; -.
DR   BioGRID-ORCS; 4478; 8 hits in 676 CRISPR screens.
DR   ChiTaRS; MSN; human.
DR   EvolutionaryTrace; P26038; -.
DR   GeneWiki; Moesin; -.
DR   GenomeRNAi; 4478; -.
DR   Pharos; P26038; Tbio.
DR   PRO; PR:P26038; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; P26038; protein.
DR   Bgee; ENSG00000147065; Expressed in lung and 253 other tissues.
DR   ExpressionAtlas; P26038; baseline and differential.
DR   Genevisible; P26038; HS.
DR   GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR   GO; GO:0045177; C:apical part of cell; IDA:BHF-UCL.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR   GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
DR   GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR   GO; GO:0071944; C:cell periphery; IDA:UniProtKB.
DR   GO; GO:0009986; C:cell surface; IDA:CAFA.
DR   GO; GO:0005737; C:cytoplasm; HDA:UniProtKB.
DR   GO; GO:0005856; C:cytoskeleton; TAS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR   GO; GO:0030175; C:filopodium; IDA:UniProtKB.
DR   GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR   GO; GO:0005902; C:microvillus; IDA:BHF-UCL.
DR   GO; GO:0031528; C:microvillus membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0031143; C:pseudopodium; IDA:UniProtKB.
DR   GO; GO:0001931; C:uropod; IEA:Ensembl.
DR   GO; GO:0031982; C:vesicle; HDA:UniProtKB.
DR   GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR   GO; GO:0050839; F:cell adhesion molecule binding; IPI:BHF-UCL.
DR   GO; GO:0003725; F:double-stranded RNA binding; IDA:MGI.
DR   GO; GO:0019899; F:enzyme binding; IPI:CAFA.
DR   GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR   GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc.
DR   GO; GO:0071394; P:cellular response to testosterone stimulus; IDA:UniProtKB.
DR   GO; GO:0061028; P:establishment of endothelial barrier; IGI:UniProtKB.
DR   GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; IMP:UniProtKB.
DR   GO; GO:0022612; P:gland morphogenesis; IMP:UniProtKB.
DR   GO; GO:0001771; P:immunological synapse formation; IDA:UniProtKB.
DR   GO; GO:0007159; P:leukocyte cell-cell adhesion; IEP:BHF-UCL.
DR   GO; GO:0050900; P:leukocyte migration; IEP:BHF-UCL.
DR   GO; GO:0022614; P:membrane to membrane docking; IEP:BHF-UCL.
DR   GO; GO:1903364; P:positive regulation of cellular protein catabolic process; IGI:UniProtKB.
DR   GO; GO:2000643; P:positive regulation of early endosome to late endosome transport; IGI:UniProtKB.
DR   GO; GO:0010628; P:positive regulation of gene expression; IGI:UniProtKB.
DR   GO; GO:0071803; P:positive regulation of podosome assembly; IEA:Ensembl.
DR   GO; GO:1902966; P:positive regulation of protein localization to early endosome; IGI:UniProtKB.
DR   GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
DR   GO; GO:0008361; P:regulation of cell size; IMP:UniProtKB.
DR   GO; GO:2000401; P:regulation of lymphocyte migration; IMP:UniProtKB.
DR   GO; GO:1902115; P:regulation of organelle assembly; IGI:UniProtKB.
DR   GO; GO:0070489; P:T cell aggregation; IDA:UniProtKB.
DR   GO; GO:0072678; P:T cell migration; IDA:UniProtKB.
DR   GO; GO:0042098; P:T cell proliferation; IDA:UniProtKB.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd13194; FERM_C_ERM; 1.
DR   Gene3D; 1.20.80.10; -; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   Gene3D; 6.10.360.10; -; 1.
DR   IDEAL; IID00344; -.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR011174; ERM.
DR   InterPro; IPR041789; ERM_FERM_C.
DR   InterPro; IPR000798; Ez/rad/moesin-like.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR   InterPro; IPR035963; FERM_2.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR019747; FERM_CS.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR018979; FERM_N.
DR   InterPro; IPR018980; FERM_PH-like_C.
DR   InterPro; IPR008954; Moesin_tail_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR23281; PTHR23281; 1.
DR   Pfam; PF09380; FERM_C; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF09379; FERM_N; 1.
DR   PIRSF; PIRSF002305; ERM; 1.
DR   PRINTS; PR00935; BAND41.
DR   PRINTS; PR00661; ERMFAMILY.
DR   SMART; SM00295; B41; 1.
DR   SMART; SM01196; FERM_C; 1.
DR   SUPFAM; SSF47031; SSF47031; 1.
DR   SUPFAM; SSF48678; SSF48678; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   PROSITE; PS00660; FERM_1; 1.
DR   PROSITE; PS00661; FERM_2; 1.
DR   PROSITE; PS50057; FERM_3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cell membrane; Cell projection; Cytoplasm;
KW   Cytoskeleton; Direct protein sequencing; Disease variant;
KW   Host-virus interaction; Membrane; Phosphoprotein; Reference proteome;
KW   S-nitrosylation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:12665801,
FT                   ECO:0000269|PubMed:1924289"
FT   CHAIN           2..577
FT                   /note="Moesin"
FT                   /id="PRO_0000219416"
FT   DOMAIN          2..295
FT                   /note="FERM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT   REGION          323..342
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          375..409
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          466..518
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           115..120
FT                   /note="[IL]-x-C-x-x-[DE] motif"
FT                   /evidence="ECO:0000305|PubMed:25417112"
FT   COMPBIAS        488..518
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         74
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         79
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         83
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P26043"
FT   MOD_RES         116
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:19690332"
FT   MOD_RES         117
FT                   /note="S-nitrosocysteine"
FT                   /evidence="ECO:0000269|PubMed:25417112"
FT   MOD_RES         139
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         165
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P26041"
FT   MOD_RES         407
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         527
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         558
FT                   /note="Phosphothreonine; by ROCK2 and STK10"
FT                   /evidence="ECO:0000269|PubMed:19255442"
FT   VARIANT         171
FT                   /note="R -> W (in IMD50; decreased protein abundance in T
FT                   cell; loss of T cell proliferation after T cell activation;
FT                   does not affect immunologic synapses formation; decreased T
FT                   cell migration in response to activation by chemokines;
FT                   increased T cell adhesion in response to activation by
FT                   integrins; dbSNP:rs1057519074)"
FT                   /evidence="ECO:0000269|PubMed:27405666"
FT                   /id="VAR_078026"
FT   MUTAGEN         115
FT                   /note="I->M: Inhibits S-nitrosylation of Cys-117; when
FT                   associated with M-120."
FT                   /evidence="ECO:0000269|PubMed:25417112"
FT   MUTAGEN         120
FT                   /note="E->M: Inhibits S-nitrosylation of Cys-117; when
FT                   associated with M-115."
FT                   /evidence="ECO:0000269|PubMed:25417112"
FT   MUTAGEN         556
FT                   /note="Y->R: Impairs phosphorylation by STK10."
FT                   /evidence="ECO:0000269|PubMed:19255442"
FT   MUTAGEN         558
FT                   /note="T->A: Abolishes phosphorylation by STK10."
FT                   /evidence="ECO:0000269|PubMed:19255442"
FT   MUTAGEN         558
FT                   /note="T->D: Completely abolishes the interaction between
FT                   N- and C-terminal domains."
FT                   /evidence="ECO:0000269|PubMed:10212266"
FT   MUTAGEN         558
FT                   /note="T->D: Phosphomimetic mutant."
FT                   /evidence="ECO:0000269|PubMed:19255442"
FT   STRAND          5..11
FT                   /evidence="ECO:0007829|PDB:1EF1"
FT   STRAND          14..20
FT                   /evidence="ECO:0007829|PDB:1EF1"
FT   HELIX           26..37
FT                   /evidence="ECO:0007829|PDB:1EF1"
FT   HELIX           42..44
FT                   /evidence="ECO:0007829|PDB:1EF1"
FT   STRAND          45..51
FT                   /evidence="ECO:0007829|PDB:1EF1"
FT   STRAND          56..58
FT                   /evidence="ECO:0007829|PDB:1EF1"
FT   STRAND          61..64
FT                   /evidence="ECO:0007829|PDB:1EF1"
FT   HELIX           65..67
FT                   /evidence="ECO:0007829|PDB:1EF1"
FT   STRAND          74..84
FT                   /evidence="ECO:0007829|PDB:1EF1"
FT   HELIX           89..92
FT                   /evidence="ECO:0007829|PDB:1EF1"
FT   HELIX           96..111
FT                   /evidence="ECO:0007829|PDB:1EF1"
FT   HELIX           119..134
FT                   /evidence="ECO:0007829|PDB:1EF1"
FT   TURN            139..141
FT                   /evidence="ECO:0007829|PDB:1EF1"
FT   TURN            144..149
FT                   /evidence="ECO:0007829|PDB:1EF1"
FT   HELIX           155..160
FT                   /evidence="ECO:0007829|PDB:1EF1"
FT   HELIX           165..178
FT                   /evidence="ECO:0007829|PDB:1EF1"
FT   TURN            179..181
FT                   /evidence="ECO:0007829|PDB:1EF1"
FT   HELIX           184..195
FT                   /evidence="ECO:0007829|PDB:1EF1"
FT   TURN            199..202
FT                   /evidence="ECO:0007829|PDB:1EF1"
FT   STRAND          204..209
FT                   /evidence="ECO:0007829|PDB:1EF1"
FT   STRAND          215..221
FT                   /evidence="ECO:0007829|PDB:1EF1"
FT   STRAND          224..229
FT                   /evidence="ECO:0007829|PDB:1EF1"
FT   STRAND          233..235
FT                   /evidence="ECO:0007829|PDB:1EF1"
FT   STRAND          237..241
FT                   /evidence="ECO:0007829|PDB:1EF1"
FT   HELIX           242..244
FT                   /evidence="ECO:0007829|PDB:1EF1"
FT   STRAND          245..251
FT                   /evidence="ECO:0007829|PDB:1EF1"
FT   STRAND          254..264
FT                   /evidence="ECO:0007829|PDB:1EF1"
FT   STRAND          267..270
FT                   /evidence="ECO:0007829|PDB:1EF1"
FT   HELIX           274..295
FT                   /evidence="ECO:0007829|PDB:1EF1"
FT   HELIX           301..343
FT                   /evidence="ECO:0007829|PDB:1E5W"
FT   HELIX           504..507
FT                   /evidence="ECO:0007829|PDB:1EF1"
FT   HELIX           511..514
FT                   /evidence="ECO:0007829|PDB:1EF1"
FT   HELIX           516..530
FT                   /evidence="ECO:0007829|PDB:1EF1"
FT   HELIX           540..550
FT                   /evidence="ECO:0007829|PDB:1EF1"
FT   HELIX           555..562
FT                   /evidence="ECO:0007829|PDB:1EF1"
FT   HELIX           567..575
FT                   /evidence="ECO:0007829|PDB:1EF1"
SQ   SEQUENCE   577 AA;  67820 MW;  865A6C5CB14AE586 CRC64;
     MPKTISVRVT TMDAELEFAI QPNTTGKQLF DQVVKTIGLR EVWFFGLQYQ DTKGFSTWLK
     LNKKVTAQDV RKESPLLFKF RAKFYPEDVS EELIQDITQR LFFLQVKEGI LNDDIYCPPE
     TAVLLASYAV QSKYGDFNKE VHKSGYLAGD KLLPQRVLEQ HKLNKDQWEE RIQVWHEEHR
     GMLREDAVLE YLKIAQDLEM YGVNYFSIKN KKGSELWLGV DALGLNIYEQ NDRLTPKIGF
     PWSEIRNISF NDKKFVIKPI DKKAPDFVFY APRLRINKRI LALCMGNHEL YMRRRKPDTI
     EVQQMKAQAR EEKHQKQMER AMLENEKKKR EMAEKEKEKI EREKEELMER LKQIEEQTKK
     AQQELEEQTR RALELEQERK RAQSEAEKLA KERQEAEEAK EALLQASRDQ KKTQEQLALE
     MAELTARISQ LEMARQKKES EAVEWQQKAQ MVQEDLEKTR AELKTAMSTP HVAEPAENEQ
     DEQDENGAEA SADLRADAMA KDRSEEERTT EAEKNERVQK HLKALTSELA NARDESKKTA
     NDMIHAENMR LGRDKYKTLR QIRQGNTKQR IDEFESM
//
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